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  • 61.12Dw  (1)
  • O-glycosylation in yeast  (1)
  • 2005-2009
  • 1990-1994  (2)
  • 1992  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied physics 54 (1992), S. 19-21 
    ISSN: 1432-0630
    Keywords: 61.12Dw ; 72.10 ; 78.50G
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The formation of silicon oxide precipitates from Czochralski grown silicon depends on the time and temperature of the heat treatment as well as on the initial content of interstitially dissolved oxygen. Samples containing between 5×1017 Oi/cm3 and 13×1017 Oi/cm3 have been heated at 750° C for 96 h. SiO2 precipitates of various shape and size have been obtained and investigated by means of small angle neutron scattering (SANS) in the Q-range 0.05 Å−1〈Q〈0.2 Å−1. The obtained SANS patterns reveal a typical anisotropy of their intensity distribution, which splits into a central peak at Q〈0.1 Å−1 due to the shape of the individual particles and a number of weak intensities for large Q-values, originating from a correlation between defects, possibly between the precipitates. While these correlation peaks in the SANS patterns are seen best for rather low values of about (5–7)×1017 Oi/cm3 oxygen content, the central peak anisotropy is most pronounced for higher values of ca 10×1017 Oi/cm3. The integrated intensity of the central peak increases with increasing initial oxygen content. For comparison, untreated samples of the same initial oxygen content do not reveal any anisotropic SAN scattering or a broadened central peak beam.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4986
    Keywords: O-glycosylation in yeast ; O-glycosylation in CHO cells ; soluble FcεRII ; methylation analysis ; sequential degradation with exoglycosidases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Recombinant human soluble low affinity receptor for the Fc portion of IgE (sFcεRII/sCD23) was produced inSaccharomyces cerevisiae or Chinese hamster ovary cells and subjected to carbohydrate analysis. Applied methods included analytical SDS-PAGE, reversed phase HPLC, methylation analysis and sequential degradation with exoglycosidases. The results revealed that sFcεRII derived from Chinese hamster ovary cells is glycosylated exclusively at Ser-147, containing mainly the trisaccharide Sia(α2–3)Gal(β1–3)GalNAc, whereas the yeast derived glycoprotein was glycosylated at Ser-167 and contained only α-mannosyl residues. It is shown here for the first time that different amino acids of a given protein can be O-glycosylated when expressed in yeast or Chinese hamster ovary cells.
    Type of Medium: Electronic Resource
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